Oral allergy syndrome (OAS) or pollen-food allergy syndrome (PFS) is a hypersensitivity reaction to specific foods due to prior sensitization to plant inhalant allergens. The relationship between seasonal allergies and food hypersensitivity was first noted in the 1940s.1 The term oral allergy syndrome was coined by Amlot et al2 in 1987 to describe oral mucosal symptoms that occasionally spread to the entire body in patients with food hypersensitivity and a positive skin test to inhalants or foods.2 Approximately 20% to 70% of patients sensitized to pollen allergens experience OAS symptoms after eating raw fruits, vegetables, nuts, or certain spices.3–6 The incidence of sensitization to plant foods is highest in those with birch pollen allergy.7 With the increasing prevalence of pollen allergies,8,9 the prevalence of OAS allergy is projected to rise. The syndrome should be suspected in patients who present with characteristic symptoms immediately after ingestion of raw fruits, nuts, vegetables, and spices. Oral allergy syndrome occurs in patients with a history of atopy, and it is thus an important phenomenon to recognize in these predisposed individuals.6,10,11
Oral allergy syndrome is triggered by a cross-reaction between allergens in pollen and allergens in fresh fruits and vegetables.12,13 Nonplant foods, such as cow’s milk, egg, or seafood, do not cause OAS. The literature is replete with reports of systemic reactions to cooked foods such as bird meat,14 chicken,15 pork,16 salami,17 as well as sensitization via mite allergens,17 attributed to OAS in the absence of a history of pollen allergy.18,19 Several authors have argued that these cases should not be included under the heading of OAS.12,19–21 Although some plant allergens that induce OAS are resistant to heating, most are heat-labile. Because digestive enzymes in the gastrointestinal tract readily break down the food allergens, most commonly in fruits, vegetables, and nuts, the symptoms of OAS are typically limited to the oropharynx, although systemic reactions may rarely occur. To avoid confusion between this unique food allergy syndrome and food allergies unrelated to inhalant allergens, the term pollen-food allergy syndrome was adopted to refer to this syndrome.12,13
Oral allergy syndrome is distinct from simple food allergies. In food allergies, a reaction develops after direct sensitization to food proteins rather than cross-reactivity between food proteins and inhalant allergens. Moreover, food allergies can be caused by plant or nonplant foods and tend to occur in response to substances that are relatively stable and able to survive gastrointestinal processing and/or cooking. In addition, food allergies more commonly result in systemic allergic reactions including anaphylaxis.
Dermatologists, allergists, and pediatricians manage a large number of patients with atopy and seasonal allergies who may also experience OAS. These patients can usually identify the fruits and vegetables that cause their symptoms. It is important for the practicing clinician to recognize these symptoms and educate those affected to avoid offending foods and mitigate rare but potential progression to more severe systemic allergic reactions.22,23 Although no case-controlled studies have been performed on the impact of food avoidance on the natural history of PFAS, identifying and avoiding foods that trigger symptoms will improve patient outcomes by lessening symptoms and increase patient safety in those with more severe allergic reactions.24,25 In addition, although dietary restriction can negatively impact patient quality of life,26 avoidance of foods that trigger symptoms remains the key in the management of OAS symptoms, particularly in those patients presenting with more severe allergic reactions.
A 12-year-old Asian boy presented with a pruritic eruption that occurred within 5 minutes after eating a red apple.27 While he was eating the apple, his hard palate started to itch, and shortly thereafter, he developed a rash around his mouth. His medical history was significant for atopic dermatitis during infancy, contact urticaria to eggplant, and seasonal allergies relieved with antihistamines. On physical examination, there were confluent urticarial erythematous patches in a perioral distribution.
A 32-year-old man presented to the Allergy and Immunology Outpatient Clinic with a chief complaint of worsening atopic dermatitis.28 His medical history was also significant for a history of perennial allergic rhinoconjunctivitis that worsened each winter and anaphylaxis to seafood, particularly lobster. He also complained of itching of his lips and throat as well as difficulty breathing after ingestion of fresh fruits, such as peaches, pears, plums, and cherries, and tree nuts including walnuts, cashews, and pistachios. His symptoms usually began 5 to 15 minutes after he ingested these foods and led him to avoid these and other fresh fruits and nuts. Skin testing showed strongly positive reactions to extracts of grasses, birch, and ragweed.
A 42-year-old lady was referred to the maxillofacial department by her general dental practitioner with a 9-month history of recurrent painful oral ulcerations.29 The pain was described as a stinging sensation on the left side of the oral cavity, her preferred side for chewing when eating. Occasionally, this was accompanied by an itchy sensation causing her to rub the areas resulting in blisters/ulcers. The onset of symptoms occurred on immediate contact with raw fruits or vegetables, including apples, melon, and raw potato. Skin prick testing with fresh fruit revealed allergies to raw apples, raw potatoes, peanuts, almonds, hazelnuts, grass, and tree pollen.
Symptoms of OAS usually occur within minutes of exposure to the offending fruits or vegetables and last from minutes to hours.28 Symptoms are typically limited to the oropharynx and are usually mild and transient. The most common symptom is oral-pharyngeal pruritus,30 especially of the lips and the palate region31; although rarely, there may also be oral and perioral angioedema.27 Patients typically describe itching or tingling in the lips or mouth, oral burning and swelling, or throat tightness after ingestion of fresh fruits or vegetables.2,32,33 Although rare, the most frequent extraoral symptoms include facial rash and nasal and otic pruritus.31 Occasionally, mucosal vesicles or blistering along the oral cavity, conjunctivitis, congestion, or coryza also occur.28,34 Physical examination may reveal tongue swelling,35 uvular edema,36 erythema and swelling of the lips,37 a perioral urticarial eruption,27 and facial38 and periorbital28 edema.
Five percent of patients have OAS progress to a more generalized allergic reaction with systemic symptoms including nausea, vomiting, abdominal pain, upper respiratory obstruction, or even anaphylaxis.12 There are currently no predictive metrics to accurately determine which patients are at risk for progression from typical OAS to systemic illness, although consumption of certain foods such as apricot, lentil, peach, and tomato have been implicated in elevating the risk in susceptible patients.39 Risk factors for systemic reactions include a history of systemic reaction to food, a positive skin prick test to commercial antigen, and prior reaction to peaches or tree nuts.12 However, oral itching after consumption of tree nuts should not be exclusively attributed to OAS because similar symptoms may herald severe systemic reactions associated with simple food allergy.12
Inhalant Allergens and Triggers
Oral allergy syndrome has been reported in response to a variety of fruits, nuts, vegetables, flowers, and spices which have been summarized, along with their most commonly associated pollinoses, in Table 1 to 3. Most studies referenced are case reports that do not indicate the botanical source of the pollen or document the part of the food (peel, pulp, seed, stem, leaf) to which the reaction occurred. Reactions can develop from small doses of triggering allergen. In some instances, OAS reactions have been reported in response to intimate or casual contact with someone who had consumed or handled the trigger.36,40 A wide variety of pollens can lead to initial sensitization and subsequent OAS. Common pollinoses include birch,39 ragweed, mugwort, grass,33 and Japanese cedar.41
The diagnosis of OAS relies on a history of oropharyngeal symptoms associated with ingestion of specific raw fruits or vegetables and pollen-associated allergies.42 Skin prick testing with the most allergenic part of the suspected fresh food (peel vs pulp) gives the most practical and reproducible results.43,44 Skin prick testing with commercial extracts has been found to be less reliable than direct inoculation with the offending agent in fresh form.45 Radioallergosorbent testing is more sensitive than skin prick testing with commercial extracts but is less sensitive than skin prick testing with fresh extracts.28 CAST-ELISA (cellular antigen stimulation test in combination with enzyme-linked immunoabsorbent assay) is more specific diagnostically for allergy to celery, hazelnut, and carrot when compared to commercial skin prick tests and allergen-specific IgE analysis.46 The CAST-ELISA is a method for assessing IgE- and non–IgE-mediated allergies.47 The test measures sulfidoleukotriene release by sensitized leukocytes after specific allergen stimulation.47 The released leukotrienes are measured by an ELISA test. A concentration of sulfidoleukotrienes greater than 200 pg/mL above the spontaneous production level is a positive result.48 Component-resolved diagnosis using microarray techniques has also been used in the diagnosis of IgE-mediated allergens, yet its utility in discriminating between sensitization versus real allergy is questionable.49 Nonetheless, it is a useful tool to analyze cross-reactivity in patients with multiple sensitizations to plant foods and pollens.50–52 However, a reliable and thorough patient history and understanding of the pollen-food associations are generally adequate for clinical diagnosis in most instances. It is important to identify those cases associated with systemic symptoms that need more extensive evaluation (Fig. 1).
Oral allergy syndrome is a type I immediate hypersensitivity reaction mediated by IgE induced by sensitization to pollen. Sensitization to pollen leads to subsequent development of cross-reactivity to food allergens. Cross-reactivity develops as a consequence of shared epitopes in the primary and tertiary structures of pollen and food allergens.13,18,53 Pollen-specific IgE antibodies are able to recognize homologous dietary allergens that share the same epitopes. The IgE allergen complexes bind to the surface of mucosal mast cells and basophils, triggering the localized release of histamine, which results in the symptoms of OAS.28
The antigenic proteins implicated in OAS have recently been classified. Many plants have developed pathogenesis-related (PR) or pathogen-response proteins to protect against pathogen invasion.28 The PR proteins have been classified into 17 families based on similarities in their physiologic properties, biological activity, and amino acid sequence (Table 4).54,55 The ribosome-inactivating proteins (PR-10), lipid transfer proteins (LTPs) (PR-14), and thaumatinlike proteins (TLPs) (PR-5) share significant homology with proteins found in various fruits and vegetables. These families of PR proteins are commonly implicated in IgE cross-reactivity resulting in OAS (Table 5).
The PR-10 proteins are the most important family of PR proteins associated with pollen-food allergy syndrome. The major birch allergen Bet v 1 is a member of this family of proteins. Birch was one of the first pollen allergies associated with hypersensitivity to various fruits and vegetables.56 A major antigenic protein in apples, Mal d 1, cross-reacts with Bet v 1 (Table 1, 5). Other fruits and vegetables with homologous proteins to Bet v 1 include the following: cherry, apricot, pear, peach, hazelnut, celery, carrot, parsley, and potato (Table 1, 2, 5).28,43 Consumption of these foods in birch-allergic individuals can lead to the symptoms of OAS. Patients with atopic dermatitis who are sensitized to birch pollen may experience a worsening of their eczema after consumption of birch pollen–related foods.57,58 Oropharyngeal reactions caused by foods that are related to birch pollen are more prevalent in central and northern Europe where birch trees are common.59
Lipid transfer proteins comprise the PR-14 family of proteins and can be found in tomatoes, peaches, apples, apricot, plum, cherry, almonds, and grapes.28,60 Lipid transfer proteins are cross-reacting antigens responsible for OAS triggered by consumption of apples and peaches in patients without birch or grass pollen allergy.28 Art v 3, the mugwort pollen LTP, has been shown to cross-react with peach LTP Pru p 3 and is involved in the mugwort/peach-associated allergy (Table 1, 2, 5).3 However, this family of proteins may also cause allergy to fruits in the absence of pollen allergy.61 The LTP microarray immunoassay data suggest that peach LTP (Pru p 3) acts as the principal primary sensitizer of food-pollen allergies and as the main gateway to polysensitization to LTPs.50 Lipid transfer proteins are particularly heat-stable and resistant to digestive enzymes, unlike most allergens causing OAS.12,62,63 Stability allows the allergen to reach the gastrointestinal immune system in an immunogenic and allergenic conformation, allowing sensitization and induction of systemic symptoms.64 Consequently, this family of proteins is more likely to cause severe systemic reactions, including urticaria, angioedema, dyspnea, and anaphylaxis.12,28,51,65 The conserved IgE-binding conformation is probably the most important factor contributing to the observation that LTP-reactive patients have a higher incidence of severe systemic reactions than classic birch-related food allergic proteins.61 Often, severe allergic reactions to LTP food allergens are triggered by physical exercise and nonsteroidal anti-inflammatory medications.51 Lipid transfer proteins are dominant allergens in the Mediterranean region and cause severe and systemic symptoms in this region at a higher rate than seen in central Europe.3,59,66
The PR-5 group of proteins has been recognized as a fairly new family of cross-reactive allergens.67 Allergens within the PR-5 group of proteins share homology with thaumatins, intensely sweet proteins first isolated from the tropical plant Thaumatococcus daniellii, native to West Africa.67 Mal d 2, the minor allergen of apple, was the first TLP described as a plant food allergen.68 Pru av 269 (a major allergen of cherry), Cup a 370 (from Cupressus arizonica pollen), Jun a 371 (from mountain cedar), and Man z TLP267 (from sapodilla plum) have also been shown to be homologous to the TLPs (Table 5). Further research is needed to understand the cross-reactivity of TLPs with other foods and pollens.
Profilin, an actin-binding protein ubiquitously present in eukaryotic cells, has also been associated with pollen- and plant-associated food allergies.72 The prevalence of skin sensitization to date-pollen-profilin has been estimated to be between 10% and 30% in pollen-allergic patients in Europe.73 In 1 study, over 50% of patients sensitized to profilins experienced oral allergy symptoms with plant-derived foods.73 However, clinical pollen-food allergy in profilin-sensitized patients may be independent of the level of specific IgE.74,75 The first profilin identified was Bet v 2, an allergen in birch pollen. IgE antibodies in birch pollen-food–allergic individuals cross-react with Bet v 2 homologous proteins from apple, pear, melon, carrot, celery, and potato (Table 1, 2, 5).28,76–78 Similarly, patients with allergies to grass pollen profilin may have OAS in response to eating peaches and apples that contain these profilin proteins.79 Patients who are sensitized to profilin tend to also be sensitized to mugwort and ragweed pollen in addition to birch and grass pollen.73 Profilin has been implicated in the mugwort-celery-spice syndrome and ragweed-melon allergy (Table 2, 3, 5).80,81 Fruit allergy to melon, watermelon, tomato, banana, pineapple, and orange may be considered a marker of profilin hypersensitivity (Table 5).73 Profilin sensitization in pollen-allergic individuals is common in southern Europe with prevalence rates of 6% in Spain’s Mediterranean coast,11 21% in Portugal,82 and 30% in Italy.73
Avoidance of known food triggers is generally the primary treatment for OAS.28,83 Avoidance of all other fresh fruits and vegetables in the same plant family, or those known to cross-react with the same pollen, may be excessively restrictive and felt to be unnecessary in most cases of OAS. Although some have suggested systematic oral challenges of fruits and vegetables that are either in the same plant family or antigenically linked to the known trigger,84 this process can be expensive and time consuming. Patients may be cautioned about the symptoms of a potentially more serious allergic reaction and maintain a list of potential cross-reactants. Patients should be alerted to proceed with caution when consuming potentially allergenic foods and be cognizant of symptoms that suggest progression to a systemic reaction (Table 1–3).
Although exclusion diets have been successful in the treatment of simple food allergies in some adults (∼1/3),85 with reports of food allergies being eliminated after strict avoidance for 2 years,86,87 food avoidance does not seem to have a role in OAS because the latter is due to cross-reaction to pollen rather than food protein. Oral allergy syndrome tends to be perennial, perhaps due to continued exposure to the corresponding and cross-reacting aeroallergens.88 Moreover, peeling the suspect foods may not provide adequate protection because the flesh may contain the provocative allergen or become contaminated during handling. However, antihistamines have been reported useful when taken before eating raw fruits and vegetables.89
Allergens in OAS typically are labile and therefore heat sensitive. Cooking suspect food is therefore 1 potential solution.90 Steam cooking kiwi for 5 minutes at 100°C has been reported to increase tolerance of kiwi in kiwi-allergic children with OAS (Table 1).91 Industrial homogenization of kiwi involving a 4-step heating process of scalding for 5 minutes at 90°C, heat treatment for 15 seconds at 115°C, stabilization for 15 seconds at 110°C, and pasteurization for 21 minutes at 65°C was also shown to eliminate kiwi sensitivity.91 Other studies have demonstrated that thermal stability of allergenic proteins in kiwi is strongly dependent on the pH.92 The antigenicity of soybean products increases at 5 minutes of boiling and gradually decreases as the duration of boiling approaches 60 minutes.93 However, diagnostic accuracy is vital in this setting because those experiencing other types of food allergy may not be protected by this exercise. Thermal processing of fruits has not been uniformly effective in decreasing their allergenicity. The disulfide bond-stabilized structure of the LTP molecule makes these proteins extremely resistant to heat denaturation.64 In addition, many foods contain both heat-stable LTPs and heat-labile PR-10 proteins (Table 6), and therefore, whether or not heating the food will result in clinical resolution of symptoms depends on which protein the patient is allergic to. Component-resolved microarray immunoassay is promising in identifying specific IgE to individual allergens, but the low sensitivity of the assay limits its utility.94 Roasted peanuts are apparently more allergenic than raw peanuts (Table 1). Roasting raw peanuts at 55°C for 10 days was shown to increase the IgE-binding activity of 2 major peanut allergens Ara h 1 and Ara h 2 as compared with raw peanuts.95 Higher allergenicity was also demonstrated with commercially roasted peanuts as compared with raw and boiled peanuts.96 More recently, autoclaving roasted peanuts at 138°C for 15 and 30 minutes has been demonstrated to produce a significant decrease of IgE-binding capacity of peanut allergens, although further studies are needed to confirm the clinical relevance of these findings.97 Hazelnuts roasted at 140°C for 40 minutes have also been shown to cause OAS in certain hazelnut-allergic patients (Table 1).98 In addition, in a subset of patients, those with OAS-like symptoms but without an aeroallergen sensitization, IgE reactivity to Mal d 3, an LTP from apple, has been shown via radioallergosorbent testing to remain unchanged despite moderate (90°C, 20 minutes) thermal treatment.99 In addition, the nonspecific LTP, Pru av 3, in cherries has been shown to retain a much higher allergenic potency after thermal processing (Table 1).100 Recombinant cherry allergens were heated at increments of 20°C, 40°C, 70°C, and 100°C during CD spectroscopy.100 In this subset of patients, therefore, heating is ineffective for prophylaxis. In addition, consumption of cooked birch-related fruits by patients with birch pollen allergy and atopic dermatitis has been implicated in flaring eczema.101 In patients with birch pollen allergy and atopic dermatitis, cooked birch-related food allergens trigger a cellular response that is not dependent on IgE binding.101 Cooked birch-related food allergens lose the capacity to bind IgE but retain their ability to activate Bet v 1–specific T-cells as native proteins and trigger atopic dermatitis.101
Although pollen immunotherapy102–104 may be efficacious in certain patients, the results are variable. A subset of birch-allergic patients with apple allergy experienced a decrease in OAS symptoms after subcutaneous injection of birch pollen extract or regular consumption of increasing amounts of the fresh apple.105–108 In addition, daily dosing of sublingual birch pollen extract solution was found to be efficacious in lessening pollen-induced allergic rhinitis and symptoms of OAS in birch-allergic patients.109 Sublingual recombinant Mal d 1 (apple PR-10 protein) and subcutaneous injection of birch pollen extract have also been shown to induce immune responses characteristic of allergen tolerance in patients with birch allergy.110,111 However, many patients do not experience improvement in their OAS symptoms, and oral food tolerance, if induced, may be only transient after immunotherapy.112–114 Further characterization of IgE epitopes of fruit allergens and greater analysis of IgE and T-cell cross-reactivity may lead to successful immunotherapies in the future.115–117
Ideally, the specific allergens causing symptoms should be easily identified in any patient; however, this is not always feasible. Fruits and vegetables may contain more than 1 allergenic protein, often from different antigenically distinct families. Individual sensitization profiles to these proteins may also vary due to dietary habits and pollinoses in each geographical area.118 In northern and central Europe, allergic reactions to plant foods are associated with birch pollen allergens Bet v 1 homologs and profilins.3 In North America, important aeroallergens include birch, rye grass, Bermuda grass, and ragweed.119 In southern Europe, allergy to fruits of the Rosaceae family is attributed to grass pollen sensitization rather than to birch pollen.79 In the Mediterranean area, LTPs are dominant allergens, whereas LTP allergy is rarely reported in central and northern Europe.3,61 Olive and Salsola pollen are largely responsible for cross-sensitizations with foods in Mediterranean regions.3,61,120 In northern China, exposure to mugwort LTP Art v 3 has been implicated in causing peach allergy,121 whereas in southern Europe, peach allergy is attributed to primary sensitization to peach LTP Pru p 3.122 Geography greatly contributes to the diagnostic complexity of pollen-food syndrome.
For patients with symptoms related to nuts, more restrictive and cautious recommendations should be suggested to prevent potentially more serious or generalized hypersensitivity reactions. Similarly, allergy to peaches and other LTP food allergens, which have also been implicated in more severe reactions, should also raise the level of caution.12 Patients with allergic rhinitis and classic OAS to other fruits and vegetables can be reassured that their symptoms are not likely to progress to anaphylaxis. Understanding the pathogenesis, triggers, management, and prognosis of OAS can enable early intervention and potentially lessen the morbidity associated with the disease.
1. Tuft L, Blumstein G. Studies in food allergy II: sensitization to fresh fruits: clinical and experimental observations. J Allergy
1942; 13( 6): 574–582.
2. Amlot PL, Kemeny DM, Zachary C, et al. Oral allergy syndrome (OAS): symptoms of IgE-mediated hypersensitivity to foods. Clin Allergy
1987; 17( 1): 33–42.
3. Flores E, Cervera L, Sanz ML, et al. Plant food allergy in patients with pollinosis from the Mediterranean area. Int Arch Allergy Immunol
2012; 159( 4): 346–354.
4. Bircher AJ, Van Melle G, Haller E, et al. IgE to food allergens are highly prevalent in patients allergic to pollens, with and without symptoms of food allergy. Clin Exp Allergy
1994; 24( 4): 367–374.
5. Osterballe M, Hansen TK, Mortz CG, et al. The prevalence of food hypersensitivity in an unselected population of children and adults. Pediatr Allergy Immunol
2005; 16( 7): 567–573.
6. Czarnecka-Operacz M, Jenerowicz D, Silny W. Oral allergy syndrome in patients with airborne pollen allergy treated with specific immunotherapy. Acta Dermatovenerol Croat
2008; 16( 1): 19–24.
7. Ballmer-Weber BK. Cutaneous symptoms after ingestion of pollen-associated foodstuffs [in German]. Hautarzt
2006; 57( 2): 108–115.
8. Bjorksten B, Clayton T, Ellwood P, et al. Worldwide time trends for symptoms of rhinitis and conjunctivitis: phase III of the International Study of Asthma and Allergies in Childhood. Pediatr Allergy Immunol
2008; 19( 2): 110–124.
9. Yura A, Kouda K, Iki M, et al. Trends of allergic symptoms in school children: large-scale long-term consecutive cross-sectional studies in Osaka Prefecture, Japan. Pediatr Allergy Immunol
2011; 22( 6): 631–637.
10. Rockmann H, van Geel MJ, Knulst AC, et al. Food allergen sensitization pattern in adults in relation to severity of atopic dermatitis. Clin Transl Allergy
2014; 4( 1): 9.
11. Huertas AJ, Carreno A, Merida C, et al. Profilin sensitisation in a Mediterranean population. Allergol Immunopathol (Madr)
2014; 42( 5): 387–394.
12. Ma S, Sicherer SH, Nowak-Wegrzyn A. A survey on the management of pollen-food allergy syndrome in allergy practices. J Allergy Clin Immunol
2003; 112( 4): 784–788.
13. Valenta R, Kraft D. Type 1 allergic reactions to plant-derived food: a consequence of primary sensitization to pollen allergens. J Allergy Clin Immunol
1996; 97( 4): 893–895.
14. Szepfalusi Z. Oral allergy syndrome related to bird meat. Allergy
1999; 54( 3): 283–284.
15. Vila L, Barbarin E, Sanz ML. Chicken meat induces oral allergy syndrome: a case report. Ann Allergy Asthma Immunol
1998; 80( 2): 195–196.
16. Asero R, Mistrello G, Falagiani P. Oral allergy syndrome from pork. Allergy
1997; 52( 6): 684–686.
17. Liccardi G, D’Amato M, D’Amato G. Oral allergy syndrome after ingestion of salami in a subject with monosensitization to mite allergens. J Allergy Clin Immunol
1996; 98( 4): 850–852.
18. Hofmann A, Burks AW. Pollen food syndrome: update on the allergens. Curr Allergy Asthma Rep
2008; 8( 5): 413–417.
19. Kelso JM. Pollen-food allergy syndrome. Clin Exp Allergy
2000; 30( 7): 905–907.
20. Boyce JA, Assa’ad A, Burks AW, et al. Guidelines for the diagnosis and management of food allergy in the United States: report of the NIAID-sponsored expert panel. J Allergy Clin Immunol
2010; 126( 6 Suppl): S1–S58.
21. Kelso JM. Oral allergy syndrome? J Allergy Clin Immunol
1995; 96( 2): 275.
22. Ortolani C, Pastorello EA, Farioli L, et al. IgE-mediated allergy from vegetable allergens. Ann Allergy
1993; 71( 5): 470–476.
23. Palgan K, Gotz-Zbikowska M, Tykwinska M, et al. Celery—cause of severe anaphylactic shock. Postepy Hig Med Dosw (Online)
2012; 66: 132–134.
24. Ando K, Watanabe D, Tamada Y, et al. Oral allergy syndrome with severe anaphylaxis induced by pistachio. Int J Dermatol
2011; 50( 5): 632–633.
25. Food allergy: a practice parameter. Ann Allergy Asthma Immunol
2006; 96( 3 Suppl 2): S1–S68.
26. Jansson SA, Heibert-Arnlind M, Middelveld RJ, et al. Health-related quality of life, assessed with a disease-specific questionnaire, in Swedish adults suffering from well-diagnosed food allergy to staple foods. Clin Transl Allergy
2013; 3: 21.
27. Chang YC, George SJ, Hsu S. Oral allergy syndrome and contact urticaria to apples. J Am Acad Dermatol
2005; 53( 4): 736–737.
28. Sloane D, Sheffer A. Oral allergy syndrome. Allergy Asthma Proc
2001; 22( 5): 321–325.
29. Rose S, Weld-Moore R, Ghazali N, et al. ‘I’ve got hay-fever and my mouth is stinging!’. Br Dent J
2011; 211( 8): 369–370.
30. Purohit-Sheth TS, Carr WW. Oral allergy syndrome (pollen-food allergy syndrome). Allergy Asthma Proc
2005; 26( 3): 229–230.
31. Bedolla-Barajas M, Morales-Romero J, Ortiz-Miramontes LR, et al. Frequency and clinical features of the oral allergy syndrome in Mexican adults with nasal pollinosis. Rev Alerg Mex
2013; 60( 1): 17–25.
32. Wuthrich B, Borga A, Yman L. Oral allergy syndrome to a jackfruit (Artocarpus integrifolia
1997; 52( 4): 428–431.
33. Anhoej C, Backer V, Nolte H. Diagnostic evaluation of grass- and birch-allergic patients with oral allergy syndrome. Allergy
2001; 56( 6): 548–552.
34. Mattila L, Kilpelainen M, Terho EO, et al. Food hypersensitivity among Finnish university students: association with atopic diseases. Clin Exp Allergy
2003; 33( 5): 600–606.
35. Ausukua M, Dublin I, Echebarria MA, et al. Oral allergy syndrome (OAS). General and stomatological aspects. Med Oral Patol Oral Cir Bucal
2009; 14( 11): e568–e572.
36. Mancuso G, Berdondini RM. Oral allergy syndrome from kiwi fruit after a lover’s kiss. Contact Dermatitis
2001; 45( 1): 41.
37. Konstantinou GN, Grattan CE. Food contact hypersensitivity syndrome: the mucosal contact urticaria paradigm. Clin Exp Dermatol
2008; 33( 4): 383–389.
38. Sanchez I, Rodriguez F, Garcia-Abujeta JL, et al. Oral allergy syndrome induced by spinach. Allergy
1997; 52( 12): 1245–1246.
39. Ortolani C, Ispano M, Pastorello E, et al. The oral allergy syndrome. Ann Allergy
1988; 61( 6 Pt 2): 47–52.
40. Wuthrich B. Oral allergy syndrome to apple after a lover’s kiss. Allergy
1997; 52( 2): 235–236.
41. Kondo Y, Tokuda R, Urisu A, et al. Assessment of cross-reactivity between Japanese cedar (Cryptomeria japonica
) pollen and tomato fruit extracts by RAST inhibition and immunoblot inhibition. Clin Exp Allergy
2002; 32( 4): 590–594.
42. Fontana M, Spertini F, Bart PA, et al. Oral allergy syndrome and food allergy [in French]. Rev Med Suisse
2005; 1( 15):1010, 1013–1017.
43. Dreborg S, Foucard T. Allergy to apple, carrot and potato in children with birch pollen allergy. Allergy
1983; 38( 3): 167–172.
44. Fernandez-Rivas M, Cuevas M. Peels of Rosaceae fruits have a higher allergenicity than pulps. Clin Exp Allergy
1999; 29( 9): 1239–1247.
45. Aleman A, Sastre J, Quirce S, et al. Allergy to kiwi: a double-blind, placebo-controlled food challenge study in patients from a birch-free area. J Allergy Clin Immunol
2004; 113( 3): 543–550.
46. Ballmer-Weber BK, Weber JM, Vieths S, et al. Predictive value of the sulfidoleukotriene release assay in oral allergy syndrome to celery, hazelnut, and carrot. J Investig Allergol Clin Immunol
2008; 18( 2): 93–99.
47. Potter PC. Clinical indications and interpretation of the CAST. Curr Allergy Clin Immunol
2006; 19( 1): 14–17.
48. Medrala W, Malolepszy J, Medrala AW, et al. CAST-ELISA test—a new diagnostic tool in pollen allergy. J Investig Allergol Clin Immunol
1997; 7( 1): 32–35.
49. Ebo DG, Bridts CH, Verweij MM, et al. Sensitization profiles in birch pollen-allergic patients with and without oral allergy syndrome to apple: lessons from multiplexed component-resolved allergy diagnosis. Clin Exp Allergy
2010; 40( 2): 339–347.
50. Palacin A, Gomez-Casado C, Rivas LA, et al. Graph based study of allergen cross-reactivity of plant lipid transfer proteins (LTPs) using microarray in a multicenter study. PLoS One
2012; 7( 12): e50799.
51. Pascal M, Munoz-Cano R, Reina Z, et al. Lipid transfer protein syndrome: clinical pattern, cofactor effect and profile of molecular sensitization to plant-foods and pollens. Clin Exp Allergy
2012; 42( 10): 1529–1539.
52. Palacin A, Rivas LA, Gomez-Casado C, et al. The involvement of thaumatin-like proteins in plant food cross-reactivity: a multicenter study using a specific protein microarray. PLoS One
2012; 7( 9): e44088.
53. Kazemi-Shirazi L, Pauli G, Purohit A, et al. Quantitative IgE inhibition experiments with purified recombinant allergens indicate pollen-derived allergens as the sensitizing agents responsible for many forms of plant food allergy. J Allergy Clin Immunol
2000; 105( 1 Pt 1): 116–125.
54. Fernandes H, Michalska K, Sikorski M, et al. Structural and functional aspects of PR-10 proteins. FEBS J
2013; 280( 5): 1169–1199.
55. Sels J, Mathys J, De Coninck BM, et al. Plant pathogenesis-related (PR) proteins: a focus on PR peptides. Plant Physiol Biochem
2008; 46( 11): 941–950.
56. Hannuksela M, Lahti A. Immediate reactions to fruits and vegetables. Contact Dermatitis
1977; 3( 2): 79–84.
57. Breuer K, Wulf A, Constien A, et al. Birch pollen-related food as a provocation factor of allergic symptoms in children with atopic eczema/dermatitis syndrome. Allergy
2004; 59( 9): 988–994.
58. Reekers R, Busche M, Wittmann M, et al. Birch pollen-related foods trigger atopic dermatitis in patients with specific cutaneous T-cell responses to birch pollen antigens. J Allergy Clin Immunol
1999; 104( 2 Pt 1): 466–472.
59. Fernandez-Rivas M, Bolhaar S, Gonzalez-Mancebo E, et al. Apple allergy across Europe: how allergen sensitization profiles determine the clinical expression of allergies to plant foods. J Allergy Clin Immunol
2006; 118( 2): 481–488.
60. Asero R, Mistrello G, Amato S. Anaphylaxis caused by tomato lipid transfer protein. Eur Ann Allergy Clin Immunol
2011; 43( 4): 125–126.
61. Zuidmeer L, van Ree R. Lipid transfer protein allergy: primary food allergy or pollen/food syndrome in some cases. Curr Opin Allergy Clin Immunol
2007; 7( 3): 269–273.
62. Masthoff LJ, Hoff R, Verhoeckx KC, et al. A systematic review of the effect of thermal processing on the allergenicity of tree nuts. Allergy
2013; 68( 8): 983–993.
63. Asero R, Mistrello G, Roncarolo D, et al. Lipid transfer protein: a pan-allergen in plant-derived foods that is highly resistant to pepsin digestion. Int Arch Allergy Immunol
2001; 124( 1-3): 67–69.
64. van Ree R. Clinical importance of non-specific lipid transfer proteins as food allergens. Biochem Soc Trans
2002; 30( Pt 6): 910–913.
65. Midoro-Horiuti T, Brooks EG, Goldblum RM. Pathogenesis-related proteins of plants as allergens. Ann Allergy Asthma Immunol
2001; 87( 4): 261–271.
66. Reuter A, Lidholm J, Andersson K, et al. A critical assessment of allergen component-based in vitro diagnosis in cherry allergy across Europe. Clin Exp Allergy
2006; 36( 6): 815–823.
67. Hegde VL, Ashok Kumar HG, Sreenath K, et al. Identification and characterization of a basic thaumatin-like protein (TLP 2) as an allergen in sapodilla plum (Manilkara zapota
). Mol Nutr Food Res
68. Oh DH, Song KJ, Shin YU, et al. Isolation of a cDNA encoding a 31-kDa, pathogenesis-related 5/thaumatin-like (PR5/TL) protein abundantly expressed in apple fruit (Nalus domestica cv. Fuji
). Biosci Biotechnol Biochem
2000; 64( 2): 355–362.
69. Dall’Antonia Y, Pavkov T, Fuchs H, et al. Crystallization and preliminary structure determination of the plant food allergen Pru av 2. Acta Crystallogr Sect F Struct Biol Cryst Commun
2005; 61( Pt 2): 186–188.
70. Cortegano I, Civantos E, Aceituno E, et al. Cloning and expression of a major allergen from Cupressus arizonica
pollen, Cup a 3, a PR-5 protein expressed under polluted environment. Allergy
2004; 59( 5): 485–490.
71. Soman KV, Midoro-Horiuti T, Ferreon JC, et al. Homology modeling and characterization of IgE binding epitopes of mountain cedar allergen Jun a 3. Biophys J
2000; 79( 3): 1601–1609.
72. Sun T, Li S, Ren H. Profilin as a regulator of the membrane-actin cytoskeleton interface in plant cells. Front Plant Sci
2013; 4: 512.
73. Asero R, Monsalve R, Barber D. Profilin sensitization detected in the office by skin prick test: a study of prevalence and clinical relevance of profilin as a plant food allergen. Clin Exp Allergy
2008; 38( 6): 1033–1037.
74. Asero R, Villalta D. Are anti-Phl p 12 IgE levels predictive of oral allergy syndrome in profilin hypersensitive patients? Eur Ann Allergy Clin Immunol
2011; 43( 6): 184–187.
75. Sirvent S, Tordesillas L, Villalba M, et al. Pollen and plant food profilin allergens show equivalent IgE reactivity. Ann Allergy Asthma Immunol
2011; 106( 5): 429–435.
76. Breiteneder H, Ebner C. Molecular and biochemical classification of plant-derived food allergens. J Allergy Clin Immunol
2000; 106( 1 Pt 1): 27–36.
77. Tordesillas L, Pacios LF, Palacin A, et al. Characterization of IgE epitopes of Cuc m 2, the major melon allergen, and their role in cross-reactivity with pollen profilins. Clin Exp Allergy
2010; 40( 1): 174–181.
78. Ebner C, Hirschwehr R, Bauer L, et al. Identification of allergens in fruits and vegetables: IgE cross-reactivities with the important birch pollen allergens Bet v 1 and Bet v 2 (birch profilin). J Allergy Clin Immunol
1995; 95( 5 Pt 1): 962–969.
79. van Ree R, Fernandez-Rivas M, Cuevas M, et al. Pollen-related allergy to peach and apple: an important role for profilin. J Allergy Clin Immunol
1995; 95( 3): 726–734.
80. Ebner C, Jensen-Jarolim E, Leitner A, et al. Characterization of allergens in plant-derived spices: Apiaceae spices, pepper (Piperaceae), and paprika (bell peppers, Solanaceae). Allergy
1998; 53( 46 Suppl): 52–54.
81. Asero R, Mistrello G, Amato S. The nature of melon allergy in ragweed-allergic subjects: a study of 1000 patients. Allergy Asthma Proc
2011; 32( 1): 64–67.
82. Tavares B, Machado D, Loureiro G, et al. Sensitization to profilin in the Central region of Portugal. Sci Total Environ
2008; 407( 1): 273–278.
83. Sabra A, Bellanti JA, Rais JM, et al. IgE and non-IgE food allergy. Ann Allergy Asthma Immunol
2003; 90( 6 Suppl 3): 71–76.
84. Crespo JF, Rodriguez J, James JM, et al. Reactivity to potential cross-reactive foods in fruit-allergic patients: implications for prescribing food avoidance. Allergy
2002; 57( 10): 946–949.
85. Barbi E, Berti I, Longo G. Food allergy: from the of loss of tolerance induced by exclusion diets to specific oral tolerance induction. Recent Pat Inflamm Allergy Drug Discov
2008; 2( 3): 212–214.
86. Clark AT, Skypala I, Leech SC, et al. British Society for Allergy and Clinical Immunology guidelines for the management of egg allergy. Clin Exp Allergy
2010; 40( 8): 1116–1129.
87. Pastorello EA, Stocchi L, Pravettoni V, et al. Role of the elimination diet in adults with food allergy. J Allergy Clin Immunol
1989; 84( 4 Pt 1): 475–483.
88. Geroldinger-Simic M, Zelniker T, Aberer W, et al. Birch pollen-related food allergy: clinical aspects and the role of allergen-specific IgE and IgG4 antibodies. J Allergy Clin Immunol
2011; 127( 3): 616.e1–622.e1.
89. Bindslev-Jensen C, Vibits A, Stahl Skov P, et al. Oral allergy syndrome: the effect of astemizole. Allergy
1991; 46( 8): 610–613.
90. Sathe SK, Teuber SS, Roux KH. Effects of food processing on the stability of food allergens. Biotechnol Adv
2005; 23( 6): 423–429.
91. Fiocchi A, Restani P, Bernardo L, et al. Tolerance of heat-treated kiwi by children with kiwifruit allergy. Pediatr Allergy Immunol
2004; 15( 5): 454–458.
92. Bublin M, Radauer C, Knulst A, et al. Effects of gastrointestinal digestion and heating on the allergenicity of the kiwi allergens Act d 1, actinidin, and Act d 2, a thaumatin-like protein. Mol Nutr Food Res
2008; 52( 10): 1130–1139.
93. Wilson S, Martinez-Villaluenga C, De Mejia EG. Purification, thermal stability, and antigenicity of the immunodominant soybean allergen P34 in soy cultivars, ingredients, and products. J Food Sci
2008; 73( 6): T106–T114.
94. Antonicelli L, Massaccesi C, Braschi MC, et al. Component resolved diagnosis in real life: the risk assessment of food allergy using microarray-based immunoassay. Eur Ann Allergy Clin Immunol
2014; 46( 1): 30–34.
95. Maleki SJ, Chung SY, Champagne ET, et al. The effects of roasting on the allergenic properties of peanut proteins. J Allergy Clin Immunol
2000; 106( 4): 763–768.
96. Mondoulet L, Paty E, Drumare MF, et al. Influence of thermal processing on the allergenicity of peanut proteins. J Agric Food Chem
2005; 53( 11): 4547–4553.
97. Cabanillas B, Maleki SJ, Rodríguez J, et al. Heat and pressure treatments effects on peanut allergenicity. Food Chem
2012; 132( 1): 360–366.
98. Hansen KS, Ballmer-Weber BK, Luttkopf D, et al. Roasted hazelnuts—allergenic activity evaluated by double-blind, placebo-controlled food challenge. Allergy
2003; 58( 2): 132–138.
99. Sancho AI, Rigby NM, Zuidmeer L, et al. The effect of thermal processing on the IgE reactivity of the non-specific lipid transfer protein from apple, Mal d 3. Allergy
2005; 60( 10): 1262–1268.
100. Scheurer S, Lauer I, Foetisch K, et al. Strong allergenicity of Pru av 3, the lipid transfer protein from cherry, is related to high stability against thermal processing and digestion. J Allergy Clin Immunol
2004; 114( 4): 900–907.
101. Bohle B, Zwolfer B, Heratizadeh A, et al. Cooking birch pollen-related food: divergent consequences for IgE- and T cell-mediated reactivity in vitro and in vivo. J Allergy Clin Immunol
2006; 118( 1): 242–249.
102. Asero R. Fennel, cucumber, and melon allergy successfully treated with pollen-specific injection immunotherapy. Ann Allergy Asthma Immunol
2000; 84( 4): 460–462.
103. Mari A, Ballmer-Weber BK, Vieths S. The oral allergy syndrome: improved diagnostic and treatment methods. Curr Opin Allergy Clin Immunol
2005; 5( 3): 267–273.
104. Kelso JM, Jones RT, Tellez R, et al. Oral allergy syndrome successfully treated with pollen immunotherapy. Ann Allergy Asthma Immunol
1995; 74( 5): 391–396.
105. Bolhaar ST, Tiemessen MM, Zuidmeer L, et al. Efficacy of birch-pollen immunotherapy on cross-reactive food allergy confirmed by skin tests and double-blind food challenges. Clin Exp Allergy
2004; 34( 5): 761–769.
106. Asero R. Effects of birch pollen-specific immunotherapy on apple allergy in birch pollen-hypersensitive patients. Clin Exp Allergy
1998; 28( 11): 1368–1373.
107. Kopac P, Rudin M, Gentinetta T, et al. Continuous apple consumption induces oral tolerance in birch-pollen-associated apple allergy. Allergy
2012; 67( 2): 280–285.
108. Okamoto Y, Kurihara K. A case of oral allergy syndrome whose symptoms were dramatically improved after rush subcutaneous injection immunotherapy with pollen extracts of birch [in Japanese]. Arerugi
2012; 61( 5): 652–658.
109. Worm M, Rak S, de Blay F, et al. Sustained efficacy and safety of a 300IR daily dose of a sublingual solution of birch pollen allergen extract in adults with allergic rhinoconjunctivitis: results of a double-blind, placebo-controlled study. Clin Transl Allergy
2014; 4( 1): 7.
110. Geroldinger-Simic M, Kinaciyan T, Nagl B, et al. Oral exposure to Mal d 1 affects the immune response in patients with birch pollen allergy. J Allergy Clin Immunol
2013; 131( 1): 94–102.
111. Mobs C, Ipsen H, Mayer L, et al. Birch pollen immunotherapy results in long-term loss of Bet v 1–specific TH2 responses, transient TR1 activation, and synthesis of IgE-blocking antibodies. J Allergy Clin Immunol
2012; 130( 5): 1108.e6–1116.e6.
112. Hansen KS, Khinchi MS, Skov PS, et al. Food allergy to apple and specific immunotherapy with birch pollen. Mol Nutr Food Res
2004; 48( 6): 441–448.
113. Asero R. How long does the effect of birch pollen injection SIT on apple allergy last? Allergy
2003; 58( 5): 435–438.
114. Mauro M, Russello M, Incorvaia C, et al. Birch-apple syndrome treated with birch pollen immunotherapy. Int Arch Allergy Immunol
2011; 156( 4): 416–422.
115. Hofmann C, Scheurer S, Rost K, et al. Cor a 1-reactive T cells and IgE are predominantly cross-reactive to Bet v 1 in patients with birch pollen-associated food allergy to hazelnut. J Allergy Clin Immunol
2013; 131( 5): 1384.e6–1392.e6.
116. Hoflehner E, Hufnagl K, Schabussova I, et al. Prevention of birch pollen-related food allergy by mucosal treatment with multi-allergen-chimers in mice. PLoS One
2012; 7( 6): e39409.
117. Twaroch TE, Focke M, Civaj V, et al. Carrier-bound, nonallergenic Ole e 1 peptides for vaccination against olive pollen allergy. J Allergy Clin Immunol
2011; 128( 1): 178.e7–184.e7.
118. Yamamoto T, Asakura K, Shirasaki H, et al. Questionnaire about the intake of and hypersensitivity to fruits, vegetables and nuts including birch pollen related foods [in Japanese]. Nihon Jibiinkoka Gakkai Kaiho
2013; 116( 7): 779–788.
119. Salo PM, Calatroni A, Gergen PJ, et al. Allergy-related outcomes in relation to serum IgE: results from the National Health and Nutrition Examination Survey 2005-2006. J Allergy Clin Immunol
2011; 127( 5): 1226.e7–1235.e7.
120. Ledesma A, Rodriguez R, Villalba M. Olive-pollen profilin. Molecular and immunologic properties. Allergy
1998; 53( 5): 520–526.
121. Gao ZS, Yang ZW, Wu SD, et al. Peach allergy in China: a dominant role for mugwort pollen lipid transfer protein as a primary sensitizer. J Allergy Clin Immunol
2013; 131( 1): 224–226.e1–3.
122. Gamboa PM, Caceres O, Antepara I, et al. Two different profiles of peach allergy in the north of Spain. Allergy
2007; 62( 4): 408–414.
123. Carnes J, Ferrer A, Fernandez-Caldas E. Allergenicity of 10 different apple varieties. Ann Allergy Asthma Immunol
2006; 96( 4): 564–570.
124. Ozcelik O, Haytac MC. Oral challenge test for the diagnosis of gingival hypersensitivity to apple: a case report. Oral Surg Oral Med Oral Pathol Oral Radiol Endod
2006; 101( 3): 317–321.
125. Pastorello EA, Ortolani C, Farioli L, et al. Allergenic cross-reactivity among peach, apricot, plum, and cherry in patients with oral allergy syndrome: an in vivo and in vitro study. J Allergy Clin Immunol
1994; 94( 4): 699–707.
126. Antico A. Oral allergy syndrome induced by chestnut (Castanea sativa
). Ann Allergy Asthma Immunol
1996; 76( 1): 37–40.
127. Perez-Ezquerra PR, de la Gaspar MV, de Fernandez MB, et al. Currant allergy and the Rosaceae-grass pollen allergy syndrome: a case report. Ann Allergy Asthma Immunol
2007; 98( 5): 480–482.
128. Kwaasi AA, Harfi HA, Parhar RS, et al. Cross-reactivities between date palm (Phoenix dactylifera L.
) polypeptides and foods implicated in the oral allergy syndrome. Allergy
2002; 57( 6): 508–518.
129. Antico A, Zoccatelli G, Marcotulli C, et al. Oral allergy syndrome to fig. Int Arch Allergy Immunol
2003; 131( 2): 138–142.
130. Guinnepain MT, Rassemont R, Claude MF, et al. Oral allergy syndrome (OAS) to grapes. Allergy
1998; 53( 12): 1225.
131. Bucher X, Pichler WJ, Dahinden CA, et al. Effect of tree pollen specific, subcutaneous immunotherapy on the oral allergy syndrome to apple and hazelnut. Allergy
2004; 59( 12): 1272–1276.
132. Lucas JS, Lewis SA, Hourihane JO. Kiwi fruit allergy: a review. Pediatr Allergy Immunol
2003; 14( 6): 420–428.
133. Egger M, Mutschlechner S, Wopfner N, et al. Pollen-food syndromes associated with weed pollinosis: an update from the molecular point of view. Allergy
2006; 61( 4): 461–476.
134. Asakura K, Yamamoto T, Shirasaki H, et al. Evaluation of relationships between foods and pollen antigens in peach oral allergy patients—serous specific IgE levels of peach recombinant Antigen [in Japanese]. Arerugi
2009; 58( 2): 133–139.
135. Liccardi G, Mistrello G, Noschese P, et al. Oral allergy syndrome (OAS) in pollinosis patients after eating pistachio nuts: two cases with two different patterns of onset. Allergy
1996; 51( 12): 919–922.
136. Rodriguez-Perez R, Crespo JF, Rodriguez J, et al. Profilin is a relevant melon allergen susceptible to pepsin digestion in patients with oral allergy syndrome. J Allergy Clin Immunol
2003; 111( 3): 634–639.
137. Ortega N, Quiralte J, Blanco C, et al. Tobacco allergy: demonstration of cross-reactivity with other members of Solanaceae family and mugwort pollen. Ann Allergy Asthma Immunol
1999; 82( 2): 194–197.
138. Hoffmann-Sommergruber K, O’Riordain G, Ahorn H, et al. Molecular characterization of Dau c 1, the Bet v 1 homologous protein from carrot and its cross-reactivity with Bet v 1 and Api g 1. Clin Exp Allergy
1999; 29( 6): 840–847.
139. Pramod SN, Venkatesh YP. Allergy to eggplant (Solanum melongena
). J Allergy Clin Immunol
2004; 113( 1): 171–173.
140. Dauby PA, Whisman BA, Hagan L. Cross-reactivity between raw mushroom and molds in a patient with oral allergy syndrome. Ann Allergy Asthma Immunol
2002; 89( 3): 319–321.
141. Kleine-Tebbe J, Vogel L, Crowell DN, et al. Severe oral allergy syndrome and anaphylactic reactions caused by a Bet v 1–related PR-10 protein in soybean, SAM22. J Allergy Clin Immunol
2002; 110( 5): 797–804.
142. Yagami A, Inaba Y, Kuno Y, et al. Two cases of pollen-food allergy syndrome to soy milk diagnosed by skin prick test, specific serum immunoglobulin E and microarray analysis. J Dermatol
2009; 36( 1): 50–55.
143. Mittag D, Vieths S, Vogel L, et al. Soybean allergy in patients allergic to birch pollen: clinical investigation and molecular characterization of allergens. J Allergy Clin Immunol
2004; 113( 1): 148–154.
144. Reider N, Sepp N, Fritsch P, et al. Anaphylaxis to camomile: clinical features and allergen cross-reactivity. Clin Exp Allergy
2000; 30( 10): 1436–1443.
145. Cadot P, Kochuyt AM, van Ree R, et al. Oral allergy syndrome to chicory associated with birch pollen allergy. Int Arch Allergy Immunol
2003; 131( 1): 19–24.
146. Figueroa J, Blanco C, Dumpierrez AG, et al. Mustard allergy confirmed by double-blind placebo-controlled food challenges: clinical features and cross-reactivity with mugwort pollen and plant-derived foods. Allergy
2005; 60( 1): 48–55.
147. Klinglmayr E, Hauser M, Zimmermann F, et al. Identification of B-cell epitopes of Bet v 1 involved in cross-reactivity with food allergens. Allergy
2009; 64( 4): 647–651.
148. de Groot H, de Jong NW, Vuijk MH, et al. Birch pollinosis and atopy caused by apple, peach, and hazelnut; comparison of three extraction procedures with two apple strains. Allergy
1996; 51( 10): 712–718.
149. Wuthrich B, Stager J, Johansson SG. Celery allergy associated with birch and mugwort pollinosis. Allergy
1990; 45( 8): 566–571.
150. Ma S, Yin J, Jiang N. Component-resolved diagnosis of peach allergy and its relationship with prevalent allergenic pollens in China. J Allergy Clin Immunol
2013; 132( 3): 764–767.
151. Lauer I, Miguel-Moncin MS, Abel T, et al. Identification of a plane pollen lipid transfer protein (Pla a 3) and its immunological relation to the peach lipid-transfer protein, Pru p 3. Clin Exp Allergy
2007; 37( 2): 261–269.
152. Palacin A, Cumplido J, Figueroa J, et al. Cabbage lipid transfer protein Bra o 3 is a major allergen responsible for cross-reactivity between plant foods and pollens. J Allergy Clin Immunol
2006; 117( 6): 1423–1429.
153. Falak R, Sankian M, Tehrani M, et al. Clinical and laboratory investigation of oral allergy syndrome to grape. Iran J Allergy Asthma Immunol
2012; 11( 2): 147–155.
154. Asero R, Pravettoni V. Anaphylaxis to plant-foods and pollen allergens in patients with lipid transfer protein syndrome. Curr Opin Allergy Clin Immunol
2013; 13( 4): 379–385.
155. Pastorello EA, Farioli L, Stafylaraki C, et al. Fennel allergy is a lipid-transfer protein (LTP)–related food hypersensitivity associated with peach allergy. J Agric Food Chem
2013; 61( 3): 740–746.
156. Asturias JA, Ibarrola I, Fernandez J, et al. Pho d 2, a major allergen from date palm pollen, is a profilin: cloning, sequencing, and immunoglobulin E cross-reactivity with other profilins. Clin Exp Allergy
2005; 35( 3): 374–381.
157. Iorio RA, Del Duca S, Calamelli E, et al. Citrus allergy from pollen to clinical symptoms. PLoS One
2013; 8( 1): e53680.
158. Diaz-Perales A, Lombardero M, Sanchez-Monge R, et al. Lipid-transfer proteins as potential plant panallergens: cross-reactivity among proteins of Artemisia pollen, Castanea nut and Rosaceae fruits, with different IgE-binding capacities. Clin Exp Allergy
2000; 30( 10): 1403–1410.
159. Palacin A, Bartra J, Munoz R, et al. Anaphylaxis to wheat flour-derived foodstuffs and the lipid transfer protein syndrome: a potential role of wheat lipid transfer protein Tri a 14. Int Arch Allergy Immunol
2010; 152( 2): 178–183.
160. Garino C, Zitelli F, Travaglia F, et al. Evaluation of the impact of sequential microwave/ultrasound processing on the IgE binding properties of Pru p 3 in treated peach juice. J Agric Food Chem
2012; 60( 35): 8755–8762.
161. Smole U, Bublin M, Radauer C, et al. Mal d 2, the thaumatin-like allergen from apple, is highly resistant to gastrointestinal digestion and thermal processing. Int Arch Allergy Immunol
2008; 147( 4): 289–298.
162. Husband FA, Aldick T, Van der Plancken I, et al. High-pressure treatment reduces the immunoreactivity of the major allergens in apple and celeriac. Mol Nutr Food Res
2011; 55( 7): 1087–1095.
163. Axelsson IG, Johansson SG, Larsson PH, et al. Characterization of allergenic components in sap extract from the weeping fig (Ficus benjamina
). Int Arch Allergy Appl Immunol
1990; 91( 2): 130–135.
164. Crespo JF, Retzek M, Foetisch K, et al. Germin-like protein Cit s 1 and profilin Cit s 2 are major allergens in orange (Citrus sinensis
) fruits. Mol Nutr Food Res
2006; 50( 3): 282–290.
165. Lopez-Rubio A, Rodriguez J, Crespo JF, et al. Occupational asthma caused by exposure to asparagus: detection of allergens by immunoblotting. Allergy
1998; 53( 12): 1216–1220.
166. Tabar AI, Alvarez-Puebla MJ, Gomez B, et al. Diversity of asparagus allergy: clinical and immunological features. Clin Exp Allergy
2004; 34( 1): 131–136.
167. Gruber P, Vieths S, Wangorsch A, et al. Maillard reaction and enzymatic browning affect the allergenicity of Pru av 1, the major allergen from cherry (Prunus avium
). J Agric Food Chem
2004; 52( 12): 4002–4007.
168. Vissers YM, Blanc F, Skov PS, et al. Effect of heating and glycation on the allergenicity of 2S albumins (Ara h 2/6) from peanut. PLoS One
2011; 6( 8): e23998.
169. Lopez-Torrejon G, Crespo JF, Sanchez-Monge R, et al. Allergenic reactivity of the melon profilin Cuc m 2 and its identification as major allergen. Clin Exp Allergy
2005; 35( 8): 1065–1072.
170. Paulsen E, Christensen LP, Andersen KE. Tomato contact dermatitis. Contact Dermatitis
2012; 67( 6): 321–327.
171. Vejvar E, Himly M, Briza P, et al. Allergenic relevance of nonspecific lipid transfer proteins 2: identification and characterization of Api g 6 from celery tuber as representative of a novel IgE-binding protein family. Mol Nutr Food Res
2013; 57( 11): 2061–2070.
172. Palacin A, Varela J, Quirce S, et al. Recombinant lipid transfer protein Tri a 14: a novel heat and proteolytic resistant tool for the diagnosis of baker’s asthma. Clin Exp Allergy
2009; 39( 8): 1267–1276.
173. Matejkova M, Zidkova J, Zidek L, et al. Investigation of thermal denaturation of barley nonspecific lipid transfer protein 1 (ns-LTP1b) by nuclear magnetic resonance and differential scanning calorimetry. J Agric Food Chem
. 2009; 57( 18): 8444–8452.
174. Asero R, Amato S, Alfieri B, et al. Rice: another potential cause of food allergy in patients sensitized to lipid transfer protein. Int Arch Allergy Immunol
2007; 143( 1): 69–74.